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Thuật ngữ y khoa chuẩn hóa theo MeSH, ICD-11, SNOMED CT.
62,341 terms indexed
A cytochrome P-450 suptype that has specificity for a broad variety of lipophilic compounds, including STEROIDS; FATTY ACIDS; and XENOBIOTICS. This enzyme has clinical significance due to its ability to metabolize a diverse array of clinically important drugs such as CYCLOSPORINE; VERAPAMIL; and MIDAZOLAM. This enzyme also catalyzes the N-demethylation of ERYTHROMYCIN.
Drugs and compounds that induce the synthesis of CYTOCHROME P-450 CYP3A.
Drugs and compounds which inhibit or antagonize the biosynthesis or actions of CYTOCHROME P-450 CYP3A.
A P450 oxidoreductase that catalyzes the hydroxylation of the terminal carbon of linear hydrocarbons such as OCTANES and FATTY ACIDS in the omega position. The enzyme may also play a role in the oxidation of a variety of structurally unrelated compounds such as XENOBIOTICS, and STEROIDS.
Drugs and compounds that induce the synthesis of CYTOCHROME P-450 ENZYMES.
Drugs and compounds which inhibit or antagonize the biosynthesis or actions of CYTOCHROME P-450 ENZYMES.
A superfamily of hundreds of closely related HEMEPROTEINS found throughout the phylogenetic spectrum, from animals, plants, fungi, to bacteria. They include numerous complex monooxygenases (MIXED FUNCTION OXYGENASES). In animals, these P-450 enzymes serve two major functions: (1) biosynthesis of steroids, fatty acids, and bile acids; (2) metabolism of endogenous and a wide variety of exogenous substrates, such as toxins and drugs (BIOTRANSFORMATION). They are classified, according to their sequence similarities rather than functions, into CYP gene families (>40% homology) and subfamilies (>59% homology). For example, enzymes from the CYP1, CYP2, and CYP3 gene families are responsible for most drug metabolism.
Cytochromes (electron-transporting proteins) in which the heme prosthetic group is heme a, i.e., the iron chelate of cytoporphyrin IX. (From Enzyme Nomenclature, 1992, p539)
Cytochromes (electron-transporting proteins) with protoheme (HEME B) as the prosthetic group.
A protein complex that includes CYTOCHROME B6 and CYTOCHROME F. It is found in the THYLAKOID MEMBRANE and plays an important role in process of PHOTOSYNTHESIS by transferring electrons from PLASTOQUINONE to PLASTOCYANIN or CYTOCHROME C6. The transfer of electrons is coupled to the transport of PROTONS across the membrane.
A group of cytochromes with covalent thioether linkages between either or both of the vinyl side chains of protoheme and the protein. (Enzyme Nomenclature, 1992, p539)
Cytochromes (electron-transporting proteins) with a tetrapyrrolic chelate of iron as a prosthetic group in which the degree of conjugation of double bonds is less than in porphyrin. (From Enzyme Nomenclature, 1992, p539)
A FLAVOPROTEIN oxidoreductase that occurs both as a soluble enzyme and a membrane-bound enzyme due to ALTERNATIVE SPLICING of a single mRNA. The soluble form is present mainly in ERYTHROCYTES and is involved in the reduction of METHEMOGLOBIN. The membrane-bound form of the enzyme is found primarily in the ENDOPLASMIC RETICULUM and outer mitochondrial membrane, where it participates in the desaturation of FATTY ACIDS; CHOLESTEROL biosynthesis and drug metabolism. A deficiency in the enzyme can result in METHEMOGLOBINEMIA.
A disease that results from a congenital defect in ELECTRON TRANSPORT COMPLEX IV. Defects in ELECTRON TRANSPORT COMPLEX IV can be caused by mutations in the SURF1, SCO2, COX10, or SCO1 genes. ELECTRON TRANSPORT COMPLEX IV deficiency caused by mutation in SURF1 manifests itself as LEIGH DISEASE; that caused by mutation in SCO2 as fatal infantile cardioencephalomyopathy; that caused by mutation in COX10 as tubulopathy and leukodystrophy; and that caused by mutation in SCO1 as early-onset hepatic failure and neurologic disorder. (from Online Mendelian Inheritance in Man, http://www.ncbi.nlm.nih.gov/Omim, MIM#220110, May 17, 2001)
A hemeprotein which catalyzes the oxidation of ferrocytochrome c to ferricytochrome c in the presence of hydrogen peroxide. EC 1.11.1.5.
Hemeproteins whose characteristic mode of action involves transfer of reducing equivalents which are associated with a reversible change in oxidation state of the prosthetic group. Formally, this redox change involves a single-electron, reversible equilibrium between the Fe(II) and Fe(III) states of the central iron atom (From Enzyme Nomenclature, 1992, p539). The various cytochrome subclasses are organized by the type of HEME and by the wavelength range of their reduced alpha-absorption bands.
A subclass of heme a containing cytochromes that have two imidazole nitrogens as axial ligands and an alpha-band absorption of 605 nm. They are found in a variety of microorganisms and in eucaryotes as a low-spin cytochrome component of MITOCHONDRIAL ELECTRON TRANSPORT COMPLEX IV.
A subclass of heme a containing cytochromes have a reduced alpha-band absorption of 587-592 nm. They are primarily found in microorganisms.
A subclass of heme a containing cytochromes with an alpha-band absorption of 605 nm. They are found in a variety of microorganisms and in eukaryotes as a high-spin cytochrome component of MITOCHONDRIAL ELECTRON TRANSPORT COMPLEX IV.
Cytochromes of the b group that have alpha-band absorption of 563-564 nm. They occur as subunits in MITOCHONDRIAL ELECTRON TRANSPORT COMPLEX III.
Cytochromes of the b group that are found bound to cytoplasmic side of ENDOPLASMIC RETICULUM. They serve as electron carrier proteins for a variety of membrane-bound OXYGENASES. They are reduced by the enzyme CYTOCHROME-B(5) REDUCTASE.
Cytochromes of the b group that are found as components of the CYTOCHROME B6F COMPLEX. They contain two non-covalently bound HEME B groups.
Cytochromes of the c type that are found in eukaryotic MITOCHONDRIA. They serve as redox intermediates that accept electrons from MITOCHONDRIAL ELECTRON TRANSPORT COMPLEX III and transfer them to MITOCHONDRIAL ELECTRON TRANSPORT COMPLEX IV.
A widely occurring subclass of c type cytochromes which function as electron carriers in the electron transport chain in photosynthetic and denitrifying BACTERIA.
The 30-kDa membrane-bound c-type cytochrome protein of mitochondria that functions as an electron donor to CYTOCHROME C GROUP in the mitochondrial and bacterial RESPIRATORY CHAIN. (From Enzyme Nomenclature, 1992, p545)
Type C cytochromes that are small (12-14 kD) single-heme proteins. They function as mobile electron carriers between membrane-bound enzymes in photosynthetic BACTERIA.
Cytochromes of the c type that are involved in the transfer of electrons from CYTOCHROME B6F COMPLEX and PHOTOSYSTEM I.
Cytochromes f are found as components of the CYTOCHROME B6F COMPLEX. They play important role in the transfer of electrons from PHOTOSYSTEM I to PHOTOSYSTEM II.
Diagnosis of the type and, when feasible, the cause of a pathologic process by means of microscopic study of cells in an exudate or other form of body fluid. (Stedman, 26th ed)
Examination of CHROMOSOMES to diagnose, classify, screen for, or manage genetic diseases and abnormalities. Following preparation of the sample, KARYOTYPING is performed and/or the specific chromosomes are analyzed.
A subdiscipline of genetics which deals with the cytological and molecular analysis of the CHROMOSOMES, and location of the GENES on chromosomes, and the movements of chromosomes during the CELL CYCLE.
A receptor subunit that is a shared component of the INTERLEUKIN-3 RECEPTOR; the INTERLEUKIN-5 RECEPTOR; and the GM-CSF RECEPTOR. High affinity receptor complexes are formed with each of these receptors when their respective alpha subunits are combined with this shared beta subunit.
A cytokine receptor that contains extracellular FIBRONECTIN TYPE III DOMAINS which mediate its function through the formation of oligomeric complexes with itself, or with a variety of CYTOKINE RECEPTORS. It does not bind IL-6, but activates JANUS KINASES and STAT3 TRANSCRIPTION FACTOR.
Mononuclear leukocytes that have been expanded in CELL CULTURE and activated with CYTOKINES such as INTERLEUKIN-2 to produce large numbers of highly cytotoxic cells.
Non-antibody proteins secreted by inflammatory leukocytes and some non-leukocytic cells, that act as intercellular mediators. They differ from classical hormones in that they are produced by a number of tissue or cell types rather than by specialized glands. They generally act locally in a paracrine or autocrine rather than endocrine manner.
The process by which the CYTOPLASM of a cell is divided.
Plant hormones that promote the separation of daughter cells after mitotic division of a parent cell. Frequently they are purine derivatives.
Methods used to study CELLS.
A genus of the family HERPESVIRIDAE, subfamily BETAHERPESVIRINAE, infecting the salivary glands, liver, spleen, lungs, eyes, and other organs, in which they produce characteristically enlarged cells with intranuclear inclusions. Infection with Cytomegalovirus is also seen as an opportunistic infection in AIDS.
Infection with CYTOMEGALOVIRUS, characterized by enlarged cells bearing intranuclear inclusions. Infection may be in almost any organ, but the salivary glands are the most common site in children, as are the lungs in adults.
Infection of the retina by cytomegalovirus characterized by retinal necrosis, hemorrhage, vessel sheathing, and retinal edema. Cytomegalovirus retinitis is a major opportunistic infection in AIDS patients and can cause blindness.